Reviewed, UniProtKB/Swiss-Prot Q9FMT1 (LEU33_ARATH)

Names and origin

Protein names

Recommended name:
    3-isopropylmalate dehydrogenase 3, chloroplastic
      Short name=3-IPM-DH 3
      Short name=IMDH 3
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase 3

Gene names

Name:	IMDH3
Ordered Locus Names:	At5g14200
ORF Names:	MUA22.20

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic activity	(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subunit structure	Homodimer By similarity.
Subcellular location	Plastid › chloroplast By similarity.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Cellular component	Chloroplast Plastid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	leucine biosynthetic process Inferred from genetic interaction. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to salt stress Inferred from expression pattern. Source: TAIR
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR
Molecular function	3-isopropylmalate dehydrogenase activity Inferred from genetic interaction. Source: TAIR NAD or NADH binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FMT1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 37	37	Chloroplast Potential
	Chain	38 – 409	372	3-isopropylmalate dehydrogenase 3, chloroplastic		PRO_0000014455
Regions
	Nucleotide binding	120 – 133	14	NAD By similarity
	Nucleotide binding	326 – 338	13	NAD By similarity
Sites
	Metal binding	268	1	Magnesium or manganese By similarity
	Metal binding	292	1	Magnesium or manganese By similarity
	Metal binding	296	1	Magnesium or manganese By similarity
	Binding site	140	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	178	1	Substrate By similarity
	Binding site	268	1	Substrate By similarity
	Site	185	1	Important for catalysis By similarity
	Site	236	1	Important for catalysis By similarity
Amino acid modifications
	Modified residue	74	1	Phosphoserine Ref.3
Experimental info
	Sequence conflict	251	1	T → A in AAL67125. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 471293D4C3FB55DD	FASTA	409	44,162
	10 20 30 40 50 60 MAAFLQTNIS LNAIKIVPGK YSSLTDHQFR APYRIRCAAA SPGKKRYNIA LLPGDGIGPE 70 80 90 100 110 120 VISVAKNVLQ KAGSLEGLEF DFKEMPVGGA ALDLVGVPLP EETFTAAKLS DAILLGAIGG 130 140 150 160 170 180 YKWDKNEKHL RPEMALFYLR RDLKVFANLR PATVLPQLVD ASTLKKEVAE GVDMMIVREL 190 200 210 220 230 240 TGGIYFGEPR GITINENGEE VGVSTEIYAA HEIDRIARVA FETARKRRGK LCSVDKANVL 250 260 270 280 290 300 DASILWRKRV TALASEYPDV ELSHMYVDNA AMQLIRDPKQ FDTIVTNNIF GDILSDEASM 310 320 330 340 350 360 ITGSIGMLPS ASLGESGPGL FEPIHGSAPD IAGQDKANPL ATILSAAMLL KYGLGEEKAA 370 380 390 400 KRIEDAVVDA LNKGFRTGDI YSPGNKLVGC KEMGEEVLKS VESKVPATV

References

[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones." Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:401-414(1997) [PubMed: 9501997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, MASS SPECTROMETRY. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB007650 Genomic DNA. Translation: BAB08299.1. AY074587 mRNA. Translation: AAL67125.1.
IPI	IPI00548301.
RefSeq	NP_196924.1.
UniGene	At.23937 At.6515 Rra.25313
3D structure databases
SMR	Q9FMT1. Positions 19-400, 47-404.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FMT1.
Proteomic databases
PRIDE	Q9FMT1.
Genome annotation databases
GeneID	831270.
GenomeReviews	Gene locus AT5G14200 in contig BA000015_GR.
NMPDR	fig|3702.1.peg.23549.
Organism-specific databases
TAIR	At5g14200.
Phylogenomic databases
HOGENOM	HBG518924.
InParanoid	Q9FMT1.
OMA	ILMIREL.
PhylomeDB	Q9FMT1.
Enzyme and pathway databases
BRENDA	1.1.1.85. 302.
Gene expression databases
Genevestigator	Q9FMT1.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004429. Isopropylmalate_DH. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit. PTHR11835:SF13. IPMDH. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00169. leuB. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEU33_ARATH

Accession

Primary (citable) accession number: Q9FMT1
Secondary accession number(s): Q8VXU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	March 1, 2001
Last modified:	February 9, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)